中性蛋白酶的单甲氧基聚乙二醇修饰  

Modification of Neutral Protease with Monomethoxypolyethylene Glycol

作　　者：张琛[1] 张瑛 郭峰[1] 李春如[3] 应明[1] 白杨[1] 王龙飞[1] 

机构地区：[1]安徽农业大学生命科学学院,合肥230036 [2]安徽省水稻遗传育种重点实验室,合肥230036 [3]安徽农业大学微生物防治省重点实验室,合肥230036

出　　处：《中国生物制品学杂志》2010年第1期79-82,共4页Chinese Journal of Biologicals

基　　金：国家高技术研究发展资助项目(863计划2007-AA021506);安徽省水稻遗传育种重点实验室开放基金SD2009-4

摘　　要：目的利用单甲氧基聚乙二醇(mPEG)化学修饰中性蛋白酶,并考察修饰酶的酶学性质。方法采用氰脲酰氯对mPEG5000进行活化,再对中性蛋白酶进行化学修饰,制得mPEG-中性蛋白酶,并比较中性蛋白酶在修饰前后的红外光谱和酶学性质。结果中性蛋白酶的修饰率为41.7%;红外光谱分析表明,修饰酶红外光谱图的多处特征峰有较大的改变;其最适温度和最适pH值未发生变化,但修饰酶的热稳定性显著提高。结论确定了经mPEG化学修饰中性蛋白酶的最适温度和最适pH值,获得的修饰酶热稳定性高于天然酶。Objective To modify neutral protease with monomethoxypolyethylene glycol（mPEG）and study the zymological property of modified protease.Methods Neutral protease was modified chemically by mPEG5000 activated with cyanuric chloride,and the infrared spectrums and zymological properties of prepared mPEG-neutral protease before and after modification were compared.Results The modification rate of neutral protease was 41.7%.Significant changes were observed in several characteristic peaks of modified neutral protease on infrared spectrum.The optimal temperature and pH value of the modified protease showed no significant changes,while the thermal stability increased significantly.Conclusion The temperature and pH value for modification of neutral protease with mPEG were optimized,and the modified protease showed high thermal stability compared with natural protease.

关 键 词：中性蛋白酶 单甲氧基聚乙二醇 化学修饰 

分 类 号：Q814[生物学—生物工程]